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A0M4D0 (PYRD_GRAFK) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotate dehydrogenase (quinone)
EC=1.3.5.2
Alternative name(s):
DHOdehase
Short name=DHOD
Short name=DHODase
Dihydroorotate oxidase
Gene names
Name:pyrD
Ordered Locus Names:GFO_2519
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Gramella

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor By similarity. HAMAP MF_00225

Catalytic activity

(S)-dihydroorotate + a quinone = orotate + a quinol. HAMAP MF_00225

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_00225

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP MF_00225

Subunit structure

Monomer By similarity. HAMAP MF_00225

Subcellular location

Cell membrane; Peripheral membrane protein By similarity HAMAP MF_00225.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCell membrane
Membrane
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological process'de novo' pyrimidine base biosynthetic process

Inferred from electronic annotation. Source: InterPro

UMP biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 340340Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_0000336468

Regions

Nucleotide binding67 – 715FMN By similarity
Nucleotide binding317 – 3182FMN By similarity
Region116 – 1205Substrate binding By similarity
Region246 – 2472Substrate binding By similarity

Sites

Active site1791Nucleophile By similarity
Binding site711Substrate By similarity
Binding site911FMN; via amide nitrogen By similarity
Binding site1431FMN By similarity
Binding site1761FMN By similarity
Binding site1761Substrate By similarity
Binding site1811Substrate By similarity
Binding site2171FMN By similarity
Binding site2451FMN; via carbonyl oxygen By similarity
Binding site2671FMN; via amide nitrogen By similarity
Binding site2961FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A0M4D0 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 52A022BE5746A488

FASTA34038,170
        10         20         30         40         50         60 
MYKSLIRPTL FKFDPEEIHY FTFNFLRKFC KIPGATSYLK SKFQVKDARL EREVFGLKFK 

        70         80         90        100        110        120 
NPVGLAAGFD KDAKLYNELS SLGFGFIEVG TVTPKPQPGN DKKRLFRLKE DSAIINRMGF 

       130        140        150        160        170        180 
NNEGVEATVN RLKSNKNVLI GGNIGKNKAT PNEHAVEDYT YSFEALFDYV NYFVVNVSSP 

       190        200        210        220        230        240 
NTPNLRELQD KEPLKDLLNT LQKKNEQKKR PKPILLKIAP DLTDEQLMDI IEIVQETKIA 

       250        260        270        280        290        300 
GVIATNTTIS REGLKSENKN EMGGLSGKPL TKRSTEVIRF LSEKSNKAFP IIGVGGIHTA 

       310        320        330        340 
EDAIEKLEAG ASLVQLYTGF IYEGPALIKD INQKILEKGL

« Hide

References

[1]"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT0803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU207366 Genomic DNA. Translation: CAL67475.1.
RefSeqYP_862542.1. NC_008571.1.

3D structure databases

ProteinModelPortalA0M4D0.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0M4D0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4650750.
GenomeReviewsGene locus GFO_2519 in contig CU207366_GR.
KEGGgfo:GFO_2519.
NMPDRfig|411154.5.peg.2381.
PATRIC22073801. VBIGraFor5527_2429.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG351027.
OMAAALNRMG.
PhylomeDBA0M4D0.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycGFOR411154:GFO_2519-MONOMER.

Family and domain databases

HAMAPMF_00225. DHO_dh_type2.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK00226.
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsTIGR01036. PyrD_sub2. 1 hit.
PROSITEPS00911. DHODEHASE_1. False negative.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_GRAFK
AccessionPrimary (citable) accession number: A0M4D0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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